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The Beclin 1 Protein Interaction Map

Autophagic responses are coupled to the activation of the inhibitor of NF-κB kinase (IKK). We report (Criollo et al. 2011, EMBO J. 30(24):4908-20) that the essential autophagy mediator Beclin 1 and TAK1-binding protein 2 and 3 (TAB2 and TAB3), two upstream activators of the TAK1-IKK signaling axis, constitutively interact with each other via their coiled-coil domains. Upon autophagy induction, TAB2 and TAB3 dissociate from Beclin 1 and bind TAK1. Moreover, overexpression of TAB2 and TAB3 suppresses, while their depletion triggers, autophagy. The expression of the C-terminal domain of TAB2 or TAB3 or that of the coiled-coil domain of Beclin 1 competitively disrupts the interaction between endogenous Beclin 1, TAB2 and TAB3, hence stimulating autophagy through a pathway that requires endogenous Beclin 1, TAK1 and IKK to be optimally efficient. These results point to the existence of an autophagy-stimulatory "switch" whereby TAB2 and TAB3 abandon inhibitory interactions with Beclin 1 to engage in a stimulatory liaison with TAK1.

Beclin 1 Pimrider displays the yeast two-Hybrid screens performed by Hybrigenics using Beclin 1 as a bait:

  1. The first one was conducted using Beclin 1 residues 46-362, a fragment previously identified in a screen for BCL-2-interacting proteins (Maiuri et al, 2007). The Beclin 1 fragement was fused to the C-terminus of LexA DNA-binding domain.
  2. The second one was conducted using full length Beclin 1 fused to the in N-terminus of LexA DNA-binding domain.

© 2012 hybrigenics